scholarly journals HMG (high-mobility-group)-14/17-like proteins in calf thyroid. Thyrotropin-dependent phosphorylation and comparison with calf thymus proteins

1983 ◽  
Vol 215 (3) ◽  
pp. 643-649 ◽  
Author(s):  
E Cooper ◽  
S W Spaulding
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
High Mobility ◽  
High Mobility Group ◽  
Group 14 ◽  
Sephadex Column ◽  
High Mobility Group Proteins ◽  
Electrophoretic Mobilities ◽  
Calf Thymus ◽  
Thymus Tissue

Two-dimensional polyacrylamide-gel electrophoresis of acid extracts of thyroid and thymus tissue, and of thyroid nuclei, revealed the presence of three HClO4-soluble nuclear proteins, PS.1, PS.2 and PS.3, whose electrophoretic mobilities closely resembled those of HMG (high-mobility-group) proteins 14 and 17. PS.1 co-migrated with HMG 14 on CM-Sephadex column chromatography. Like HMG 14, PS.2 and PS.3 were phosphorylated in calf thyroid slices; 32P-labelling of PS.3 was stimulated by thyrotropin. Thyrotropin also induced a rapid increase in the labelling of A5, an HMG-14/17-like protein found in whole calf thyroid and thymus tissue, but not in thyroid nuclei.

scholarly journals Studies on the tissue specificity of the high-mobility-group non-histone chromosomal proteins from calf

1978 ◽  
Vol 173 (2) ◽  
pp. 497-505 ◽  
Author(s):  
A Rabbani ◽  
G H Goodwin ◽  
E W Johns
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Trichloroacetic Acid ◽  
Tissue Specificity ◽  
Polyacrylamide Gel Electrophoresis ◽  
High Mobility ◽  
Acid Precipitation ◽  
High Mobility Group ◽  
Chromosomal Proteins ◽  
Calf Thymus

The high-mobility-group (HMG) non-histone chromosomal proteins from calf thymus, liver, spleen and kidney were extracted, and fractionated by CM-Sephadex chromatography and trichloroacetic acid precipitation. The isolated proteins HMG 1, HMG 2 and HMG 17 from the tissues were compared by polyacrylamide-gel electrophoresis, isoelectric focusing and amino acid analysis. The results show that the three proteins are very similar in the tissues studied, implying a lack of tissue specificity.

scholarly journals Heterogeneity of high-mobility-group protein 2. Enrichment of a rapidly migrating form in testis

1985 ◽  
Vol 229 (1) ◽  
pp. 233-240 ◽  
Author(s):  
L R Bucci ◽  
W A Brock ◽  
M L Meistrich
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
High Mobility ◽  
Polyacrylamide Gel ◽  
High Mobility Group ◽  
Lymphoid Tissues ◽  
Rat Tissues ◽  
High Mobility Group Protein ◽  
Group Protein ◽  
Testis Tissue

A determination of the absolute amounts of high-mobility-group proteins 1 and 2 (HMG1 and HMG2) in rat tissues demonstrated that amounts of HMG2 were low in non-proliferating tissues, somewhat higher in proliferating and lymphoid tissues, but were extremely elevated in the testis. This increase was due to a germ-cell-specific form of HMG2 with increased mobility relative to somatic HMG2 on acid/urea/polyacrylamide-gel electrophoresis. To determine if the findings in the rat were a general feature of spermatogenesis, testis (germinal), spleen (lymphoid), and liver (non-proliferating) tissues from various vertebrate species were examined for their relative amounts of HMG1 and HMG2, and for HMG2 heterogeneity. Bull, chimpanzee, cynomologus monkey, dog, gopher, guinea pig, hamster, mouse, opossum, rabbit, rat, rhesus monkey, squirrel and toad (Xenopus) tissues were analysed. Nearly all species showed relatively high contents of HMG2 in testis tissue, whereas HMG1 contents were similar in all species and tissues. Ten of thirteen species showed a rapidly migrating HMG2 subtype in testis tissue, separable by acid/urea/polyacrylamide-gel electrophoresis. Xenopus, which lacks HMG2 in somatic tissues, showed an HMG2-like protein in testis tissue. Although the rapidly migrating HMG2 subtype in species other than rat was not testis-specific, it was always enriched in the testis. This study indicates that increased amounts of HMG2 and the enrichment of a rapidly migrating HMG2 subtype are general features of spermatogenic cells.

Structural Studies on Two High-Mobility-Group Proteins from Calf Thymus, HMG-14 and HMG-20 (Ubiquitin), and Their Interaction with DNA

2005 ◽  
Vol 112 (3) ◽  
pp. 577-580 ◽  
Author(s):  
Peter D. CARY ◽  
Deborah S. KING ◽  
Colyn CRANE-ROBINSON ◽  
E. Morton BRADBURY ◽  
Azra RABBANI ◽  
...  
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
Structural Studies ◽  
High Mobility Group Proteins ◽  
Calf Thymus

scholarly journals Studies on the high-mobility-group non-histone proteins from hen oviduct

1979 ◽  
Vol 181 (3) ◽  
pp. 585-591 ◽  
Author(s):  
C S Teng ◽  
G K Andrews ◽  
C T Teng
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
High Mobility ◽  
High Mobility Group ◽  
Micrococcal Nuclease ◽  
Hmg Proteins ◽  
Deoxyribonuclease I ◽  
Micrococcal Nuclease Digestion ◽  
Calf Thymus ◽  
Nuclease Digestion ◽  
Limited Digestion

Nuclear high-mobility-group (HMG) proteins were isolated from hen oviduct. These were proteins HMG-1, −2, −3, −14 and −17, which are equivalent to the classification of calf thymus HMG proteins. Hen oviduct proteins HMG-1 and −2 were individually isolated by HCIO4.extraction and CM-Sephadex chromatographic separation. Their mol.wts. were determined as 28 000 and 27 000, respectively. The proteins have a high content of acidic and basic amino acids. The association of proteins HMG-1 and −2 with the genome of hen oviduct nuclei was probed by a limited digestion with nucleases. Hen oviduct nuclei were incubated with deoxyribonuclease I or micrococcal nuclease until 10% of the DNA was digested. The nuclear suspension was centrifuged and the contents of proteins HMG-1 and −2 in the supernatant and sediment fractions were analysed by polyacrylamide-gel electrophoresis. HMG proteins were found to be preferentially released by micrococcal-nuclease digestion rather than by deoxyribonuclease I.

scholarly journals Two new low-molecular-weight acidic proteins from calf thymus nuclei that resemble HMG (high-mobility-group) proteins 14 and 17

1982 ◽  
Vol 207 (3) ◽  
pp. 519-527 ◽  
Author(s):  
P D Cary
Keyword(s):  
Molecular Weight ◽  
Tertiary Structure ◽  
High Mobility ◽  
High Mobility Group ◽  
Proton Nuclear Magnetic Resonance ◽  
High Mobility Group Proteins ◽  
Calf Thymus ◽  
Hydrophobic Amino Acids ◽  
Thymus Nucleus ◽  
Acidic Proteins

Two new, closely similar, acidic proteins were extracted and purified from calf thymus and designated AP-X and AP-Y (acidic proteins X and Y). They contain about 33% acidic residues, mostly non-amidated, and 20% lysine, but no arginine, tyrosine, histidine or tryptophan. There is a single phenylalanine residue in a molecular weight of approx. 5000. Circular dichroism and proton nuclear magnetic resonance show that they do not take up secondary or tertiary structure in free solution, as expected from the low content of hydrophobic amino acids. They appear structurally related to the high-mobility-group proteins HMG 14 and 17. Controlled extraction experiments indicate that proteins AP-X and AP-Y are at least partially located in the calf thymus nucleus.

ADP-ribosylation of histones and acid-soluble, high mobility group like chromosomal proteins from Physarum polycephalum

1987 ◽  
Vol 65 (1) ◽  
pp. 81-85 ◽  
Author(s):  
G. G. Poirier ◽  
Serge Coté ◽  
Dominic Pallotta
Keyword(s):  
Gel Electrophoresis ◽  
Physarum Polycephalum ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Chromosomal Proteins ◽  
Cellular Slime Mould ◽  
Adp Ribosylation ◽  
Cellular Slime

Nuclei from the cellular slime mould Physarum polycephalum were incubated with [32P]NAD. The chromosomal basic proteins were acid extracted and separated by two-dimensional polyacrylamide gel electrophoresis. After autoradiography the poly(ADP-ribosylated) proteins were identified. Histone H1 was the major acceptor. Histones H2B and H2A were significantly modified, although to a lesser extent than H1. In addition, the acid-soluble, high mobility group-like proteins AS-2 and AS-3 and the protein A-24 showed some modification. Histones H3 and H4 were not modified. The pattern of ADP-ribosylation did not change with NAD concentrations between 1 and 100 μM NAD.

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